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Information on EC 1.11.1.10 - chloride peroxidase and Organism(s) Leptoxyphium fumago and UniProt Accession P04963
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1.11.1.10 chloride peroxidaseIUBMB Comments
Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.
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Word Map
- 1.11.1.10
- fumago
-
caldariomyces
- horseradish
-
chlorination
- peroxidases
-
halogen
- halide
- haloperoxidase
-
bromination
- lactoperoxidase
- inaequalis
-
ferryl
-
curvularia
-
soret
-
bromoperoxidase
- monochlorodimedone
-
low-spin
-
p450cam
-
vanadium-dependent
- thioanisole
-
peroxidase-catalyzed
-
thiolate-ligated
- pyrrocinia
-
oxoferryl
- n,n-dimethylaniline
-
peroxygenases
-
agrocybe
-
vanadium-containing
-
hypohalous
- aegerita
- degradation
- synthesis
- environmental protection
- biotechnology
The taxonomic range for the selected organisms is: Leptoxyphium fumago
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
chloroperoxidase, cpo-i, chloride peroxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chloroperoxidase
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CPO
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Chloride peroxidase
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-
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chloroperoxidase
CPO
peroxidase, chloride
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Vanadium chloride peroxidase
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vCPO
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additional information
chloroperoxidase
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-
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chloroperoxidase
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CPO
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CPO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RH + chloride + H2O2 = RCl + 2 H2O
substrate specificity and reaction mechanism, overview. Relative favorability of catalytic epoxidation and allylic hydroxylation of olefins, a type of alkene oxidation selectivity. The selectivity for epoxidation versus can be rationalized in terms of the proximal pocket's modulation of the thiolate's electron push and consequent influence on the heme redox potential and the basicity of the trans ligand
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Achmatowicz-type ring expansion
the oxidative conversion of alpha-heterosubstituted furfuryl derivatives to six-membered O- or N-heterocyclic building blocks
redox reaction
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-
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oxidation
reduction
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oxidation
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SYSTEMATIC NAME
IUBMB Comments
chloride:hydrogen-peroxide oxidoreductase
Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols.
CAS REGISTRY NUMBER
COMMENTARY
9055-20-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chlorodimedone + chloride + H2O2
1,1-dimethyl-4,4-dichloro-3,5-cyclohexanedione + 2 H2O
model substrate monochlorodimedone
-
-
?
alizarin red S + Cl- + H+ + H2O2
? + 2 H2O
98.2% efficiency, degradation to nine different products
-
-
?
crystal violet + Cl- + H+ + H2O2
? + 2 H2O
97.7% efficiency, degradation to three products
-
-
?
estradiol + 2 bromide + 2 H2O2
2,4-bromo beta-estradiol + 4 H2O
-
-
-
?
estradiol + 2 chloride + 2 H2O2
2,4-dichloro beta-estradiol + 4 H2O
-
-
-
?
estradiol + chloride + H2O2
2-chloro beta-estradiol + 2 H2O
-
-
-
?
estradiol + chloride + H2O2
4-chloro beta-estradiol + 2 H2O
-
-
-
?
RH + chloride + H2O2
RCl + 2 H2O
-
-
-
?
thymol + Br- + H2O2
3-bromothymol + 4-bromothymol + 6-bromothymol + H2O
-
-
-
?
(1R,2S)-(+)-2-benzylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(+)-2-benzyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(+)-2-ethylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-2-ethyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(+)-2-methylcyclopropanemethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-2-methyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(+)-2-propylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-(-)-1-formyl-2-propylcyclopropane + ?
-
-
-
-
?
(1R,2S)-(-)-2-acetoxymethylcyclopropylmethanol + tert-butyl hydroperoxide
(1S,2R)-2-acetoxymethyl-1-formylcyclopropane + ?
-
-
-
-
?
(1R,2S)-cyclohexa-3,5-diene-1,2-diyl diacetate + tert-butyl hydroperoxide
(1S,2S,3S,6S)-7-oxabicyclo[4.1.0]hept-4-ene-2,3-diyl diacetate + (1R,2S,5R,6S)-5,6-dihydroxycyclohex-3-ene-1,2-diyl diacetate + ?
-
-
-
-
?
(1S)-3-carene + Cl- + H2O2
(1S,3R,4R,6R)-4-chloro-3,7,7-trimethyl-bicyclo[4.1.0]heptane-3-ol + H2O
-
-
-
-
?
(2E)-hex-2-en-1-ol + tert-butyl hydroperoxide
trans-(3-propyloxiran-2-yl)methanol + H2O
-
-
-
-
?
(2Z)-hex-2-en-1-ol + tert-butyl hydroperoxide
cis-(3-propyloxiran-2-yl)methanol + H2O
-
-
-
-
?
(2Z)-pent-2-en-1-ol + tert-butyl hydroperoxide
cis-2-(3-ethyloxiran-2-yl)ethanol + (3Z)-hex-3-enal + H2O
-
-
-
-
?
(3E,5E)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4E)-6-oxohepta-2,4-dienal + (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one + (2E)-4-oxopent-2-enal
-
-
83% (2E,4E)-6-oxohepta-2,4-dienal, 4% (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one, and 13% (2E)-4-oxopent-2-enal
-
?
(3Z,5E)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4Z)-6-oxohepta-2,4-dienal + (2E)-4-oxopent-2-enal + (2E,4E)-6-oxohepta-2,4-dienal
-
-
78% (2E,4Z)-6-oxohepta-2,4-dienal, 15% (2E)-4-oxopent-2-enal and 7% (2E,4E)-6-oxohepta-2,4-dienal
-
?
(3Z,5Z)-hepta-3,5-dien-2-one + tert-butyl hydroperoxide
(2E,4Z)-6-oxohepta-2,4-dienal + (2E)-4-oxopent-2-enal + (3Z)-4-[(2S,3S)-3-methyloxiran-2-yl]but-3-en-2-one
-
-
27% (2E,4Z)-6-oxohepta-2,4-dienal, 38% (3E)-4-(3-methyloxiran-2-yl)but-3-en-2-one and 35% (3Z)-4-[(2S,3S)-3-methyloxiran-2-yl]but-3-en-2-one
-
?
(4Z)-hex-4-en-1-ol + tert-butyl hydroperoxide
3-(3-methyloxiran-2-yl)propan-1-ol + (4Z)-hex-4-enal + H2O
-
-
-
-
?
(5R,6S)-5,6-dimethoxycyclohexa-1,3-diene + tert-butyl hydroperoxide
(1S,4S,5S,6S)-4,5-dimethoxy-7-oxabicyclo[4.1.0]hept-2-ene + ?
-
-
-
-
?
(R)-limonene + H2O2
(1S,2S,4R)-limonene-1,2-diol + (1R,2R)-4R-limonene-1,2-diol + ?
-
when the reaction is carried out in the presence of chloride ions an enhancement in the reaction rate is observed, maintaining the regioselectivity, but not the stereoselectivity. The reaction products under these conditions are (1S,2S)-4R-limonene-1,2-diol and (1R,2R)-4R-limonene-1,2-diol. In the presence of potassium chloride the limonene oxidation also occurs by the produced hypochlorite without stereoselectivity
-
-
?
(R)-limonene + H2O2
(1S,2S,4R)-limonene-1,2-diol + H2O
-
in the absence of chloride ions, at pH 3 or pH 6, the reaction is regio and stereoselective with a diasteromeric excess of more than 99% of (1S,2S)-4R-limonene-1,2-diol
-
-
?
1,2-dihydronaphthalene + tert-butyl hydroperoxide
(1R,2R)-dihydroxytetrahydronaphthalene + ?
-
-
-
-
?
1,3-cycloheptadiene + tert-butyl hydroperoxide
(1R,3R)-cyclohept-3-ene-1,2-diol + (1R,4S)cyclohept-2-ene-1,4-diol + (1R,4R)-cyclohept-2-ene-1,4-diol + ?
-
-
-
-
?
1,3-cyclooctadiene + tert-butyl hydroperoxide
cycloocta-1,4-dien-1-yl hydroperoxide + cycloocta-2,4-dien-1-ol + ?
-
-
main product is cycloocta-1,4-dien-1-yl hydroperoxide, formation of small amounts of cycloocta-2,4-dien-1-ol
-
?
2 pyrene + 3 KCl + 3 H2O2
chloropyrene + dichloropyrene + 3 KOH + 3 H2O
-
-
-
-
?
2'-deoxyuridine + Br- + H2O2
5-bromo-2'-deoxyuridine + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + HCl
?
-
-
-
-
?
2,3,5,6-tetrachloroaniline + HCl + H2O2
pentachloroaniline + H2O
-
the main product from peroxidase oxidation is a polymeric and insoluble material
-
-
?
2,3,5,6-tetrachlorophenol + HCl + H2O2
pentachlorophenol + H2O
-
the main product from peroxidase oxidation is a polymeric and insoluble material
-
-
?
2,4,6-trichlorophenol + H2O2
2,6-dichloro-1,4-benzoquinone + H2O + HCl
-
-
-
-
?
2-methyl-4-propylcyclopentane-1,3-dione + Cl- + H2O2
2-chloro-2-methyl-4-propylcyclopentane-1,3-dione + H2O
-
reaction without appreciable stereoselectivity
-
?
3-amino-1-propanol + tert-butyl hydroperoxide
3-aminopropanal + H2O + ?
-
83.6% conversion
-
-
?
4,6-dimethyldibenzothiophene + Cl- + H2O2
?
-
the substrate exists as a monomeric and dimeric species in aqueous acetonitrile solutions. Oxidation of dimer substrate is preferred when compared to monomer oxidation
-
-
?
5-hexen-1-ol + tert-butyl hydroperoxide
5-hexenal + ?
-
-
only a small amount is produced
-
?
7-azaindole + H2O2
7-azaoxindole + H2O
-
cross-linked enzyme aggregates
-
-
?
acenaphthene + Cl- + H2O2
dichloroacenaphthene + trichloroacenaphthene + H2O
-
-
-
?
anthracene + 2 KCl + 2 H2O2
9,10-dichloroanthracene + 2 KOH + 2 H2O
-
-
-
-
?
benzyl-N-(2-hydroxyethyl)-carbamate + tertbutyl hydroperoxide
Cbz-glycinal + ?
-
-
-
-
?
benzyloxycarbonyl ethanolamine + tert-butyl hydroperoxide
benzyloxycarbonyl glycinal
-
-
-
-
?
biphenylene + Cl- + H2O2
dichlorobiphenylene + trichlorobiphenylene + H2O
-
-
-
?
Boc-D-methionine-methyl ester + H2O2
Boc-D-methionine-methyl ester sulfoxide + H2O
-
-
-
-
?
Boc-L-methionine-methyl ester + H2O2
Boc-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
-
i.e. monochlorodimedone
-
-
?
cis-2-hexen-1-ol + tert-butyl hydroperoxide
cis-2-hexenal + ?
-
-
further production of small amounts of trans-2-hexenal, cis-3-hexenal and trans-3-hexenal
-
?
cis-3-hexen-1-ol + tert-butyl hydroperoxide
cis-3-hexenal + ?
-
-
further production of small amounts of cis-2-hexenal, trans-2-hexenal and trans-3-hexenal
-
?
cis-4-hexen-1-ol + tert-butyl hydroperoxide
cis-4-hexenal + cis-4,5-epoxyhexan-1-ol + ?
-
-
further production of small amounts of trans-4,5-epoxyhexan-1-ol and trans-4-hexenal
-
?
cis-beta-methylstyrene + chloride + H2O2
?
-
-
the enzyme produced (1S2R)- and (1R2S)-epoxides at a 96:4 product ratio
-
?
cis-cyclohexa-3,5-diene-1,2-diol + tert-butyl hydroperoxide
(1R,2S,3S,4S)-cyclohex-5-ene-1,2,3,4-tetrol + ?
-
-
+ traces of (1R,2S,3S,6S)-7-oxabicyclo[4.1.0]hept-4-ene-2,3-diol
-
?
isoplagiochin C + Cl- + H2O2
?
-
incorporation of 1-6 chlorine atoms
-
-
?
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
-
-
-
-
?
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
-
-
-
-
?
monochlorodimedone + Cl- + H2O2
dichlorodimedone + H2O
-
-
-
-
?
N-acetyl-L-methionine-methyl ester + H2O2
N-acetyl-L-methionine-methyl ester (RS)-sulfoxide
-
-
-
-
?
N-Cbz-3-amino-1-propanol + H2O2
N-Cbz-3-aminopropanal + H2O
-
9.7% conversion
-
-
?
N-Cbz-3-amino-1-propanol + tert-butyl hydroperoxide
N-Cbz-3-aminopropanal + H2O + ?
-
10.9% conversion
-
-
?
N-Cbz-5-aminopentanol + H2O2
N-Cbz-5-aminopentanal + H2O
-
16.3% conversion
-
-
?
N-Cbz-5-aminopentanol + tert-butyl hydroperoxide
N-Cbz-5-aminopentanal + H2O + ?
-
16.8% conversion
-
-
?
N-Cbz-6-aminohexanol + H2O2
N-Cbz-6-aminohexanal + H2O
-
12.3% conversion
-
-
?
N-Cbz-6-aminohexanol + tert-butyl hydroperoxide
N-Cbz-6-aminohexanal + H2O + ?
-
9.4% conversion
-
-
?
N-chloroacetyl-L-methionine-methyl ester + H2O2
N-chloroacetyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-formyl-L-methionine-methyl ester + H2O2
N-formyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-ethionine-methyl ester + H2O2
N-methoxycarbonyl-D-ethionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-ethyl ester + H2O2
N-methoxycarbonyl-D-methionine-ethyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-methyl ester + H2O2
N-methoxycarbonyl-D-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-n-butyl ester + H2O2
N-methoxycarbonyl-D-methionine-n-butyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-D-methionine-n-propyl ester + H2O2
N-methoxycarbonyl-D-methionine-n-propyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-ethionine-ethyl ester + H2O2
N-methoxycarbonyl-L-ethionine-ethyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-ethionine-methyl ester + H2O2
N-methoxycarbonyl-L-ethionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-ethyl ester + H2O2
N-methoxycarbonyl-L-methionine-ethyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-methyl ester + H2O2
N-methoxycarbonyl-L-methionine-methyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-butyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-butyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-pentyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-pentyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
N-methoxycarbonyl-L-methionine-n-propyl ester + H2O2
N-methoxycarbonyl-L-methionine-n-propyl ester (RS)-sulfoxide + H2O
-
-
-
-
?
pentachlorophenol + HCl + H2O
?
-
the main product from peroxidase oxidation is a polymeric and insoluble material
-
-
?
styrene + H2O2
?
-
native enzyme is conjugated with polystyrene to form a surfactant-like structure that self assembled at oil-water interfaces. The interface-assembly of the enzyme improves the overall catalytic efficiency as compared to traditional biphasic reactions with enzymes contained in bulk aqueous phase. The interfacial placement of the enzyme can suppress unwanted side reactions including the hydrolysis of the styrene epoxide product
-
-
?
sulfur mustard + chloride + H2O2
sulfur mustard sulfoxide + H2O
-
-
-
-
?
thioanisole + HCl + H2O2
?
-
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
-
-
?
thymine + Br- + H2O2
5-bromo-6-hydroxy-5,6-dihydrothymine + H2O
-
-
-
?
trans-2-hexen-1-ol + tert-butyl hydroperoxide
trans-2-hexenal + ?
-
-
further production of small amounts of cis-2-hexenal,cis-3-hexenal and trans-3-hexenal
-
?
trans-2-phenylcyclopropylmethanol + tert-butyl hydroperoxide
?
-
formation of the aldehyde with poor enantioselectivity
-
-
?
trans-3,4-dimethoxycinnamic acid + Br- + H2O2 + H+
DL-1,1-dibromo-2-hydroxy-2-(3,4-dimethoxy-5-bromophenyl)ethane + DL-1,1-dibromo-2-hydroxy-2-(3,4-dimethoxyphenyl)ethane + 2-bromo-3-hydroxy-3-(3,4-dimethoxyphenyl)propionic acid + H2O
-
-
-
?
trans-3,4-dimethoxycinnamic acid + Cl- + H2O2 + H+
trans-1-chloro-2-(3,4-dimethoxy-5-chlorophenyl)ethylene + trans-1-chloro-2-(3,4-dimethoxyphenyl)ethylene + DL-1,1-dichloro-2-hydroxy-2-(3,4-dimethoxyphenyl)ethane
-
-
-
?
trans-3-hexen-1-ol + tert-butyl hydroperoxide
trans-3-hexenal + ?
-
-
further production of small amounts of cis-3-hexenal, trans-2-hexenal and cis-3-hexenal
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-2-(3-ethyloxiran-2-yl)ethanol + (3E)-hex-3-enal + H2O
-
-
-
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-4,5-epoxyhexan-1-ol + trans-4-hexenal + H2O + ?
-
-
-
-
?
trans-4-hexen-1-ol + tert-butyl hydroperoxide
trans-4-hexenal + trans-4,5-epoxyhexan-1-ol + ?
-
-
further production of small amounts of cis-4,5-epoxyhexan-1-ol and cis-4-hexenal
-
?
trans-4-hydroxycinnamic acid + Br- + H+ + H2O2
trans-1-bromo-2-(4-hydroxyphenyl)ethylene + H2O
-
-
-
?
trans-4-hydroxycinnamic acid + Cl- + H+ + H2O2
trans-1-chloro-2-(4-hydroxyphenyl)ethylene + H2O
-
-
-
?
trans-4-methoxy-cinnamic acid + Br- + H+ + H2O2
2,3-dihydroxy-3-(4-methoxyphenyl)propionic acid + DL-1,1-dibromo-2-hydroxy-2-(4-methoxyphenyl)ethane + H2O
-
-
-
?
trans-cinnamic acid + H2O2 + Br- + H+
trans-1-bromo-2-phenylethylene + erythro-2-bromo-3-hydroxy-3-phenylpropionic acid + H2O
-
-
-
?
tyrosine + Cl- + H2O2
monochlorotyrosine + dichlorotyrosine
-
-
-
?
[2-(2-bromoethyl)cyclopropyl]methanol + tert-butyl hydroperoxide
2-(2-bromoethyl)cyclopropanecarbaldehyde + ?
-
-
-
-
?
[2-(3-bromopropyl)cyclopropyl]methanol + tert-butyl hydroperoxide
2-(3-bromopropyl)cyclopropanecarbaldehyde + ?
-
-
-
-
?
[2-(hydroxymethyl)cyclopropyl]methyl acetate + tert-butyl hydroperoxide
(2-formylcyclopropyl)methyl acetate + ?
-
-
-
-
?
[3.2.0]hept-2-en-6-one + Br- + H2O2
(1S,2S,3S,5S)-3-bromo-2-hydroxybicyclo[3.2.0]heptan-6-one + H2O
-
-
-
?
monochlorodimedon + chloride + H2O2
dichlorodimedon + 2 H2O
-
-
-
?
monochlorodimedon + chloride + H2O2
dichlorodimedon + 2 H2O
H2O2 activation of the heme group
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + H2O2
? + H2O
-
24.4% conversion
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + H2O2
? + H2O
-
25.7% conversion
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + tert-butyl hydroperoxide
? + H2O
-
18.8% conversion
-
-
?
benzyl N-(2-hydroxyethyl)carbamate + tert-butyl hydroperoxide
? + H2O
-
77.9% conversion
-
-
?
indole + H2O2
2-oxoindole + H2O
-
chloroperoxidase at neutral and at acidic pH is able to catalytically scavenge peroxynitrite, although the reaction cycle is not fully clarified
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
-
?
additional information
?
-
production of polyhalogenated carbazoles (PHCs) from halogenation of carbazole in the presence of bromide and/or chloride under the catalysis of chloroperoxidase (CPO) isolated from the marine fungus Caldariomyces fumago, see also EC 1.11.1.18. A total of 25 congeners including mono-to tetra-substituted chlorinated, brominated, and mixed halogenated carbazoles (with substitution patterns of -BrCl, -BrCl2, -BrCl3, -Br2Cl, -Br2Cl2, and -Br3Cl) are produced from the reactions under various conditions. The PHC product profiles are apparently dependent on the halide concentrations. In the CPO-mediated chlorination of carbazole, 3-mono- and 3,6-dichlorocarbazoles predominated in the formation products. In addition to the less abundant mixed halogenated carbazoles (-Br2Cl), 1,3,6-tri- and 1,3,6,8-tetrabromocarbazoles are the dominant products in reactions containing both Br- and Cl-
-
-
-
additional information
?
-
the immobilized enzyme CPO catalyzes degradation of mesotrione (2-[(4-methylsulfonyl)-2-nitrobenzoyl]cyclohexan-1,3-dione) in wastewater
-
-
-
additional information
?
-
asymmetric sulfoxidation of 2-(diphenylmethylthio) acetamide to (R)-modafinil
-
-
-
additional information
?
-
chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz-type ring expansion. In combination with glucose oxidase as oxygen-activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6-hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase-driven aerobic activation, extended enzyme half-lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six-membered O-heterocycles. The chloroperoxidase from Caldariomyces fumago (CPO) acts as peroxidase-P450 functional hybrid. Enantiodiscrimination in the oxidative conversion of racemic furfuryl alcohols by enzyme CPO in a coupled assay with the glucose oxidase (GOx) from Aspergillus niger, substrate specificity, overview
-
-
-
additional information
?
-
CPO is a haeme-thiolate peroxidase requiring the presence of H2O2 to form an activated enzymatic species, responsible for oxidising either halides or organic substrates. CPO catalyses the halogenation of estrogens at comparable rates to other aromatic compounds
-
-
-
additional information
?
-
CPO-catalyzed degradation of the dyes Orange G, acid blue 45, or crystal violet from wastewater samples, kinetics at pH 3.0, 20°C
-
-
-
additional information
?
-
LC-MS/MS and gas chromatography-mass spectrometry (GC-MS) are used for product identification, overview. Hydroxylated polybrominated diphenyl ethers (diOH-PBDEs) and hydroxylated polybrominated biphenyls (diOH-PBBs) formed by dihydroxyl group substitutions in the ortho-positions relative to the diphenyl ether bond or the single bond in biphenyl, may undergo intramolecular cyclization
-
-
-
additional information
?
-
theoretical analysis of the influence of the proximal pockets of cytochrome P450CAM and chloroperoxidase (CPO) on the relative favorability of catalytic epoxidation and allylic hydroxylation of olefins, a type of alkene oxidation selectivity. Quantum mechanical models of the active site are employed to isolate the proximal pocket's influence on the barrier for the selectivity-determining step for each reaction, using cyclohexene and cis-beta-methylstyrene as substrates. The proximal pocket shows preference for epoxidation, the largest value being for CPO, converting the active heme-thiolate moiety from being intrinsically hydroxylation-selective to being intrinsically epoxidation-selective. The proximal pocket is the key determinant of alkene oxidation selectivity. The selectivity for epoxidation can be rationalized in terms of the proximal pocket's modulation of the thiolate's electron push and consequent influence on the heme redox potential and the basicity of the trans ligand. The ratio of epoxidation to allylic hydroxylation products [C=C/C-H ratio or alkene oxidation selectivity (AOS)] is measured for several substrates, including propene, 2-butene, cyclohexene, and cis-beta-methylstyrene (CBMS), for catalysis by CPO or P450 isozymes, e.g. oxidation reactions of cyclohexene with compound I. The AOS varies according to substrate and enzyme, on average, epoxidation is slightly favored. The substrates studied lack strongly orienting interactions with residues of the distal binding pocket, consequently, the intrinsic reactivity of the heme-thiolate group with these substrates may make a significant contribution, perhaps the dominant one, to the AOS of P450 and CPO toward them
-
-
-
additional information
?
-
-
in the absence of organic substrates, chloroperoxidase catalyzes the peroxidation of chloride and bromide ion to molecular chlorine and bromine. However these molecular species are not formed as intermediates in the enzymic halogenation of organic halogen-acceptor substrates
-
-
?
additional information
?
-
-
oxidation of phenolics and related compounds with H2O2
-
-
?
additional information
?
-
-
oxidation of substituted indoles and sulfides with H2O2
-
-
?
additional information
?
-
-
peroxidation of para-substituted phenolic compounds
-
-
?
additional information
?
-
-
evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
-
-
?
additional information
?
-
-
the enzyme also catalyzes peroxidase and catalase reaction in the absence of halide substrates
-
-
?
additional information
?
-
-
catalyzes the oxidation iodide to iodine
-
-
?
additional information
?
-
-
the enzyme also catalyzes the dismutation of chlorine dioxide into chloride, chlorate and oxygen
-
-
?
additional information
?
-
-
transformation of aromatic pollutants into chlorinated derivatives by microbial enzymes may occur in polluted sites. This biocatalytic process should be considered because the toxicity and environmental impact of aromatic compounds may be increased
-
-
?
additional information
?
-
-
in halide-independent oxidation reactions, CPO uses H2O2 or other organic peroxides as the source of oxygen without requiring cofactors
-
-
?
additional information
?
-
-
no reaction with N-acetyl-L-methionine, N-methoxycarbonyl-L-methionine, N-phthaloyl-L-methionine
-
-
?
additional information
?
-
-
a mechanistic comparison between cytochrome P450- and chloroperoxidase-catalyzed N-dealkylation of N,N-dialkyl anilines
-
-
?
additional information
?
-
-
catalyzes the unspecific chlorination, bromination, and iodation (but no fluorination) of a variety of electrophilic organic substrates via hypohalous acid as actual halogenating agent. In the absence of halide, CPO resembles cytochrome P450s and epoxidizes and hydroxylates activated substrates such as organic sulfides and olefins. Aromatic rings are not susceptible to CPO-catalyzed oxygen-transfer
-
-
?
additional information
?
-
-
crystal structure of the reaction intermediate compound 0 determined at a resolution of 1.75 A
-
-
?
additional information
?
-
-
in the presence of enzyme and H2O2, but in the absence of chloride or bromide, the terpene alcohols geraniol, nerol and citronellol are substrates of CPO and are oxidized to the corresponding aldehydes geranial, neral and citronellal, respectively
-
-
?
additional information
?
-
-
the enzyme can dehalogenate trihalophenols and p-halophenols. CCPO catalyzes H2O2-dependent defluorination, debromination, and deiodination reactions. Two main products, p-benzoquinone (minor) and the halophenol dimer (major), are observed for all p-halophenol-CCPO-catalyzed dehalogenation reactions
-
-
?
additional information
?
-
-
exhibits catalase, peroxidase and cytochrome P450 activities besides the halogenation reaction
-
-
?
additional information
?
-
-
oxidation of hydrophobic substrates in alpha-pinene-based ternary systems using tert-butyl hydroperoxide (compound/main product: cis-2-heptene/cis-2-heptene oxide, 1-methyl-cyclohexene/1-methyl-1,2-dihydroxycyclohexane, geraniol/geranial, nerol/neral, perillyl alcohol/perillyl aldehyde)
-
-
?
additional information
?
-
-
oxidative dehalogenation of trihalophenols and p-halophenols
-
-
?
additional information
?
-
-
CPO is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase-, catalase-, and cytochrome P450-type reactions of dehydrogenation, hydrogen peroxide decomposition, and oxygen insertion, respectively
-
-
?
additional information
?
-
-
the enzyme is incapable of catalyzing the halogenation of indole
-
-
?
additional information
?
-
-
formation and protonation of compound X, a hypochlorite heme adduct intermediate existing during CPO-catalyzed halide-dependent reactions, significantly lowers the reaction barrier and increases the efficiency of CPO-catalyzed orange G degradation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-chlorodimedone + chloride + H2O2
1,1-dimethyl-4,4-dichloro-3,5-cyclohexanedione + 2 H2O
model substrate monochlorodimedone
-
-
?
monochlorodimedon + chloride + H2O2
dichlorodimedon + 2 H2O
-
-
-
?
RH + chloride + H2O2
RCl + 2 H2O
-
-
-
?
additional information
?
-
production of polyhalogenated carbazoles (PHCs) from halogenation of carbazole in the presence of bromide and/or chloride under the catalysis of chloroperoxidase (CPO) isolated from the marine fungus Caldariomyces fumago, see also EC 1.11.1.18. A total of 25 congeners including mono-to tetra-substituted chlorinated, brominated, and mixed halogenated carbazoles (with substitution patterns of -BrCl, -BrCl2, -BrCl3, -Br2Cl, -Br2Cl2, and -Br3Cl) are produced from the reactions under various conditions. The PHC product profiles are apparently dependent on the halide concentrations. In the CPO-mediated chlorination of carbazole, 3-mono- and 3,6-dichlorocarbazoles predominated in the formation products. In addition to the less abundant mixed halogenated carbazoles (-Br2Cl), 1,3,6-tri- and 1,3,6,8-tetrabromocarbazoles are the dominant products in reactions containing both Br- and Cl-
-
-
-
additional information
?
-
the immobilized enzyme CPO catalyzes degradation of mesotrione (2-[(4-methylsulfonyl)-2-nitrobenzoyl]cyclohexan-1,3-dione) in wastewater
-
-
-
additional information
?
-
-
transformation of aromatic pollutants into chlorinated derivatives by microbial enzymes may occur in polluted sites. This biocatalytic process should be considered because the toxicity and environmental impact of aromatic compounds may be increased
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
heme
-
-
348310, 348311, 348313, 671523, 671543, 676907, 685220, 695865, 695975, 699596, 699770, 699777, 712511, 712645, 712791, 724183, 725740, 725782
heme
-
binding of the para-substituted phenolic compounds close to the heme
heme
-
the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
heme
-
formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
additional information
the CPO prosthetic group is Fe (IV) protoporphyrin
-
additional information
the enzyme involves the protoporphyrin prosthetic group with the pI range of 3.2-4.0
-
additional information
-
the enzyme does not require any cofactor for its activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
maximum activity at a ratio of 2 mol M3+/mol of enzyme. Inhibitory above a ratio of 4 mol M3+/mol of enzyme
Cd2+
maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme
Cr3+
maximum activity at a ratio of 2 mol M3+/mol of enzyme. Inhibitory above a ratio of 4 mol M3+/mol of enzyme
Cu2+
maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme
Fe2+
Fe3+
maximum activity at a ratio of 2 mol M3+/mol of enzyme. Inhibitory above a ratio of 4 mol M3+/mol of enzyme
La3+
maximum activity at a ratio of 2 mol M3+/mol of enzyme. Inhibitory above a ratio of 4 mol M3+/mol of enzyme
Mn2+
maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme
Pb2+
maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme
Zn2+
maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme
Fe
Fe2+
in CPO, the sulfur atom in the Cys29 is located at the appropriate distance from the amide group of the Leu 32 and Glu 51 that leads to the hydrogen bonding formation of the amidesulfur groups, which is important for metalloproteins for the iron alignment
Fe
-
existence of an Fe(IV)OH species in chloroperoxidase compound II (reaction intermediate)
Fe
-
the reaction intermediate compound 0 is present in the ferric low-spin doublet ground state and is characterized by a long O-O bond length of 1.5 A and a Fe-O bond distance of 1.8 A
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl dicarbonate
-
the covalent modification of His105 inhibits the epoxidation and peroxide dismutations catalyzed by CPO
dimethyl dicarbonate
-
the covalent modification of His105 inhibits the epoxidation and peroxide dismutations catalyzed by CPO
hydrogen peroxide
-
the main process leading to peroxide-mediated enzyme inactivation is heme destruction (all tryptophan residues are partially oxidized in the inactive protein). 80000 molar equivalents of hydrogen peroxide are sufficient to reduce the activity of CPO to less than 5%
Sodium cyanoborohydride
-
activity decreases in 38.2 and 92.6% for sodium cyanoborohydride molar excess of 1:1000 and 1:10000
additional information
-
not inhibited by sodium cyanoborohydride in molar excess of 1:10 and 1:100
-
azide
-
active site ligand and inhibitor. At pH 4.0, supra-micromolar concentrations of azide inhibit the enzyme activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
enhances total turnover number compared to reaction without antioxidant
azide
-
at pH 4.0, infra-micromolar concentrations of azide enhance enzyme activity
caffeic acid
-
the total turnover number is almost 5fold higher than that obtained for the reference reaction
cetyltrimethylammonium bromide
-
the peroxidation activity of CPO is enhanced by 248% while oxidation activity is enhanced by 215% in cetyltrimethylammonium bromide reverse micelle medium
citraconic anhydride
-
the catalytic efficiency of the modified enzyme for sulfoxidation in aqueous buffer is increased by 26.2%
dodecyltrimethylammonium bromide
-
the peroxidation activity of CPO is enhanced by 263%, while oxidation activity is enhanced by 222% in dodecyltrimethylammonium bromide medium
ferulic acid
-
enhances total turnover number compared to reaction without antioxidant
Maleic anhydride
-
the catalytic efficiency of the modified enzyme for sulfoxidation in aqueous buffer is increased by 22.6%
phthalic anhydride
-
the catalytic efficiency of the modified enzyme for sulfoxidation in aqueous buffer is increased by 12.9%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0048
beta-estradiol
with Br-, pH 3.0, temperature not specified in the publication
0.0066
beta-estradiol
with Cl-, pH 3.0, temperature not specified in the publication
0.152
equiline
with Br-, pH 3.0, temperature not specified in the publication
-
0.216
equiline
with Cl-, pH 3.0, temperature not specified in the publication
-
0.0033
estrone
with Br-, pH 3.0, temperature not specified in the publication
0.0066
estrone
with Cl-, pH 3.0, temperature not specified in the publication
1.14
H2O2
-
pH 3.0, 25°C, immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
0.0261
Monochlorodimedon
-
free enzyme, in citrate buffer (50 mM, pH 3.0) at 25°C
0.0277
Monochlorodimedon
-
bio-conjugated enzyme, in citrate buffer (50 mM, pH 3.0) at 25°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetic analysis of free and immobilized enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics at pH 3.0, 20°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33
beta-estradiol
with Cl-, pH 3.0, temperature not specified in the publication
420
beta-estradiol
with Br-, pH 3.0, temperature not specified in the publication
1930
equiline
with Cl-, pH 3.0, temperature not specified in the publication
-
1970
equiline
with Br-, pH 3.0, temperature not specified in the publication
-
120
estrone
with Cl-, pH 3.0, temperature not specified in the publication
330
estrone
with Br-, pH 3.0, temperature not specified in the publication
123
4,6-dimethyldibenzothiophene
-
aqueous solution containing 5% acetonitrile
209.3
4,6-dimethyldibenzothiophene
-
aqueous solution containing 40% acetonitrile
653.4
4,6-dimethyldibenzothiophene
-
aqueous solution containing 20% acetonitrile
661.1
4,6-dimethyldibenzothiophene
-
aqueous solution containing 30% acetonitrile
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5000
beta-estradiol
with Cl-, pH 3.0, temperature not specified in the publication
87500
beta-estradiol
with Br-, pH 3.0, temperature not specified in the publication
8935
equiline
with Cl-, pH 3.0, temperature not specified in the publication
-
12960
equiline
with Br-, pH 3.0, temperature not specified in the publication
-
18181
estrone
with Cl-, pH 3.0, temperature not specified in the publication
100000
estrone
with Br-, pH 3.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.4 - 3
-
soluble enzyme and immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
2.7
-
the extremely acidic optimal reaction pH suggests the protonation of a residue, presumably, Glu 183 in CPO catalysis
2.8
3
-
free and bio-conjugated-CPO poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
2 - 4
-
pH 2.0: about 60% of maximal acticity of soluble enzyme, about 65% of maximal activity of immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads). pH 4.0: about 55% of maximal activity of soluble enzyme, about 75% of maximal activity of immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
2 - 5
-
free and bio-conjugated-CPO poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane
3 - 4
-
at pH values lower than 3.0 or higher than 4.0, the enzyme is completely inhibited
3.7 - 7
-
pH 3.7: about 90% of maximal activity, soluble and immobilized enzyme. pH 7.0: about 55% of maximal activity of immobilized enzyme, about 50% of maximal activity of soluble enzyme
3 - 7
activity range for CPO-catalyzed halogenation of carbazole, preferential formation of higher substituted bromocarbazoles under acidic conditions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
40
-
immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
35
-
free and bio-conjugated-CPO poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 90
degradation of crystal violet, more than 80% of maximum activity
20 - 60
degradation of alizarin red S, more than 60% of maximum activity
20 - 50
20 - 50
-
20°C: about 45% of maximal activity of soluble enzyme, about 65% of maximal activity of immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads), 50°C: about 35% of maximal activity of soluble enzyme, about 65% of maximal activity of immobilized enzyme (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads)
20 - 50
-
free and bio-conjugated-CPO poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme involves the protoporphyrin prosthetic group with the pI range of 3.2-4.0
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Removal of the sugars from CPO leads to increase the hydrophobicity of the enzyme, as well as the reduction of the alkylation reactions
physiological function
additional information
evolution
Caldariomyces fumago chloroperoxidase (CPO) is a glycosylated hemoprotein enzyme from the peroxidase family
evolution
chloroperoxidase (CPO) is a glycosidic hemoprotein enzyme of the peroxidase family
evolution
chloroperoxidase (CPO) is a hybrid of two different families of enzymes, peroxidases and P450s
physiological function
chloroperoxidase (CPO) is a heme-thiolate enzyme able to catalyse the halogenation and oxidation of a wide range of organic substrates. CPO-catalysed chlorination and bromination reaction of natural estrogens, beta-estradiol, estrone and equiline are efficiently converted to halogenated compounds in the presence of chloride or bromide and hydrogen peroxide. The bromination reaction proceeds more efficiently than the chlorination reaction. Three major products are detected for chlorination of beta-estradiol, two of them are monohalogenated compounds while a third product is a dihalogenated compound at positions 2 and 4 of the aromatic ring A. Chlorinated compounds are not substrates for tyrosinase, suggesting that the halogenated form of estrogens is less susceptible to form o-quinones. Chlorinated estradiol is not a substrate of tyrosinase. Whereas E2 is completely consumed in the presence of tyrosinase, E2-derived chlorinated compounds are not transformed. 2,4-Dichloroestradiol is 90fold less estrogenic compared to beta-estradiol
physiological function
chloroperoxidase (CPO), secreted by the marine fungus Caldariomyces fumago, is a versatile enzyme with the capacity to catalyze the incorporation of halogen atoms into organic molecules in the presence of peroxides such as H2O2. Production of polyhalogenated carbazoles (PHCs) from halogenation of carbazole in the presence of bromide and/or chloride under the catalysis of chloroperoxidase (CPO) isolated from the marine fungus Caldariomyces fumago. CPO-catalyzed halogenation of carbazole may play an important role in the natural formation of PHCs. PHCs exhibit dioxin-like toxicity and are persistent and bioaccumulative. PHCs induce cytochrome P450 enzymes and certain other enzyme activities. The chlorinated and brominated carbazoles produced in the reactions with Cl- and Br- in vitro are also found in aquatic environments, overview
physiological function
chloroperoxidase (CPO), which is a versatile heme-containing enzyme, can catalyze sulfoxidation, epoxidation, dismutation, halogenation, and oxidation of numerous compounds with extensive high regioselectivity and enantioselectivity
physiological function
containing both a P450-like proximal pocket and a peroxidase-like distal pocket, enzyme chloroperoxidase (CPO) is a versatile heme-containing enzyme that possesses the catalytic capacities of both peroxidase and P450 enzyme families. CPO has multiple catalytic functions, attributable to four CPO-mediated processes, including bromination, radical coupling, intramolecular cyclization and debromination. Phenol is readily transformed into a variety of brominated organic compounds (BOCs) via the CPO-mediated oxidative process. Higher bromide concentrations and lower pH conditions both facilitate the formation of brominated products. While a higher bromination capacity is observed in pH 3.0 solutions, CPO-mediated radical couplings are more favorable at pH 5.0 and pH 6.0. Although CPO might catalyze chlorination when chloride and bromide coexisted in the solution, BOCs are the dominant products of CPO-mediated phenol oxidation. Bromination (EC 1.11.1.18) is preferable to chlorination (EC 1.11.1.10) in the CPO-mediated reaction in the presence of both bromide and chloride
physiological function
the heme-containing CPO exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing the halogenation reactions. CPO selectively causes the oxidation and epoxidation of the diverse chemical compounds through the specific stereochemistry mechanism
physiological function
the immobilized enzyme CPO catalyzes degradation of mesotrione (2-[(4-methylsulfonyl)-2-nitrobenzoyl]cyclohexan-1,3-dione) in wastewater
additional information
analysis of the effect of 1-butyl-3-methylimidazolium bromide ([BMIM][Br]) and 1-butyl-3-methylimidazolium methyl sulfate ([BMIM] [MeSO4]) ionic liquids on the structure and function of chloroperoxidase (CPO) by molecular dynamics (MD) simulation using the enzyme structure (PDB ID 2CPO) as template, detailed overview. [BMIM][MeSO4] possesses greater influence on the enzyme structure, because of the special structure of the corresponding anion group. Besides, the number of cavities interprets the activation of the enzyme at the low concentrations and its inactivation at the high concentrations. The penetration of the anions into the enzyme structure is confirmed at the high concentrations of the ionic liquids. The role of ionic liquids at low concentrations is related to their binding to the enzyme structure. Their role at the high concentrations depends on the changes in the solvent arrangement as well as the attachment to the enzyme. Low concentration of ionic liquid play an important role and cause higher chloroproxidase activity.Whereas in high concentration due to surface coating of chloroproxidase by ionic liquid, despite the access of the substrate to the active site, CPO activity decreases. In chloroperoxidase, the substrate accesses the active site and heme group through a small channel above heme
additional information
computational molecular dynamics calculation, simulation, and modeling, using the glycosylated enzyme structure PDB ID 2CPO, overview
additional information
substrate specificity via hybrid quantum mechanics/molecular mechanics (QM/MM) calculation and simulation, modeling and structure-function analysis, overview. The influence of the NH-S hydrogen bonds on the full reaction profiles for hydroxylation and epoxidation has been studied by density functional theory (DFT) calculations on small heme-thiolate models that incorporate ammonia molecules hydrogen bonded to a proximal SH- group. The proximal pocket is the key determinant of alkene oxidation selectivity. The selectivity for epoxidation can be rationalized in terms of the proximal pocket's modulation of the thiolate's electron push and consequent influence on the heme redox potential and the basicity of the trans ligand. Creation of two active-site models for each substrate/enzyme combination, one with a bare heme-thiolate and one that also includes the proximal pocket, so that comparison of the PES's reveals the influence of the proximal pocket on the intrinsic reactivity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRXC_LEPFU
373
0
40504
Swiss-Prot
Secretory Pathway (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
glycoprotein
chloroperoxidase (CPO) is a glycosidic hemoprotein enzyme
glycoprotein
CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Analysis of the effects of the sugar segments on the structure and activity of CPO through the simulation of the halo structure and the structures without the sugar segment, overview. According to molecular dynamics simulation (MD), seven channels and fifteen cavities are identified in the CPO structure. Two of the channels provide the substrate access to the active site. The MD simulation results reveal that the removal of NAG decreases the number of the cavities from fifteen to eleven. Besides, the removal of NAG is associated with removing the channel providing the substrate access. The number of the cavities decreases from fifteen to fourteen through the removal of MAN, but, channel providing the substrate access to the active site is partly preserved. The MD simulation results indicate that the structures without the sugar units are more compact in comparison with the halo structures. The removal of the sugar segments induces the significant changes in the flexibility of the residues that affect the catalytic activity of the enzyme. As a result, the enzyme activities, such as the oxidation, alkylation, halogenation, and epoxidation cannot occur when the sugar segments of the enzyme are removed
glycoprotein
-
the chloroperoxidase gene encodes three potential glycosylation sites
glycoprotein
-
heavily glycosylated protein (2530% carbohydrates, two high-mannose N-glycosylation sites)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate
-
sitting drop vapor diffusion method, crystals are modified by several cross-linkers, but only glutaraldehyde is able to produce catalytically active and insoluble crystals. Although the cross-linked crystals are catalytically active, they show lower specific activity than the soluble enzyme
-
structure model comparison of isoforms CPO and CPO2, high conservation of the active site and the substrate channel. Amino acids Cys30, Met62, Met154 and Trp226 of CPO, which are oxidized upon treatment of the enzyme with a CPO-inactivating H 2 O 2 concentration, are also contained in CPO2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E183H
-
the mutation is detrimental to the chlorination and dismutation activity of chloroperoxidase, activities are reduced by 85% and 50% of the wild-type activity. Epoxidation activity of the mutant enzyme is significantly enhanced, about 2.5fold
additional information
additional information
chloroperoxidase is successfully entrapped in multi polysaccharide magnetic supports, which are developed based on a multi polysaccharide shell. Leakage of the enzyme is observed with single-shell polysaccharide coating. High CPO reusability is measured with a polymeric double-shell magnetic microsupport. The magnetic cores contain iron oxide nanoparticles, the polymer diminishes the interaction between the magnetic cores themselves, can improve the colloidal stability of the support, and prevent any interaction with the environment that would affect both support properties and enzyme stability. Different magnetic micro-supports, based on polydopamine-coated iron oxide nanoparticles with a multi polysaccharide shell, are developed and evaluated. Method overview. CPO is successfully immobilized with an efficiency of entrapment between 92% and 100% in the case of supports with chitosan in the interior or outer shell respectively. A very good chemical stability of the support under reaction conditions is observed in the case of an interior shell of alginate and an outer coating of chitosan, together with an excellent reusability of the immobilized enzyme, that is recycled to catalyze up to 25 consecutive reaction cycles. Chlorination of monochlorodimedone to dichlorodimedone is used as model reaction for chloroperoxidase catalytic assay
additional information
development of an immobilization method for chloroperoxidase (CPO) via carbohydrate-binding lectin protein, concanavalin A (ConA). ConA is attached on the surface of silica-coated magnetic nanoparticles (MNPs) for effective recovery (ConA/Fe3O4-SiO2). CPO shows about 100% activity recovery after its immobilization on ConA functionalized MNPs. After storing for four weeks, the immobilized CPO still maintains 80% activity while only 46% of activity of free enzyme is retained. Immobilized CPO by biometric magnetic nanoparticles exhibits excellent reusability and enantioselectivity in asymmetric synthesis of modafinil. More than 82% of original conversion rate and 70% enantiomeric excess (ee) value are observed after being run eight times. Synthesis and characterization of the ConA-functionalized magnetic nanoparticles, overview. CPO is fixed in the surface of nanoparticles without steric limitation and exposed to medium as free CPO. The immobilization temperature has little effect on immobilization efficiency, but CPO lost its activity at high temperature (>40°C). Meanwhile, CPO has a high immobilization efficiency at acidic conditions, but its activity greatly decreases at pH 7.0. Maximum immobilization efficiency and relative activity for immobilized CPO is obtained at 20°C and pH 6.0. ConA can efficiently conserve the natural activity of original CPO during the immobilization
additional information
enhancement of the catalytic performance of chloroperoxidase by co-immobilization with glucose oxidase (GOx) on magnetic graphene oxide (MGO), the catalytic efficiency (kcat/Km) of CPO immobilized on either MGO or MGO-GOx is approximately 2.1 and 2.5times higher, respectively, compared to that of the free CPO. The superior catalytic enzymes chloroperoxidase and glucose oxidase are co-immobilized onto the surface of MGO, method development and evaluation, overview. Graphene oxide/iron oxide (MGO) composites functionalized with Fe3O4 nanoparticles, providing the magnetic property, are used. The magnetism of the composites allows easy separation of the enzyme for reuse while the unique surface property of the composites significantly enhances the catalytic performance of the enzyme. The catalytic efficiency of immobilized CPO is much higher than that of free CPO. Immobilized CPO can be effectively and conveniently recovered and is ready to reuse. Enzyme cascade helps to harness the power of enzymes requiring auxiliary proteins. MGO-GOx-CPO reaches its peak activity (95.2%) when temperature is maintained between 42°C and 50°C compared to the optimal temperature of 35°C for the free enzyme. MGO-GOx-CPO reuse shows a good recovery in the presence of an external magnetic field, with about 38.5% activity remaining after 6 cycles of applications
additional information
immobilization of chloroperoxidase, method development, detailed overview. Halloysite nanotube (HNT) is a natural bio-compatible and stable nanomaterial available in abundance at low-cost. HNT is modified by two strategies to make it suitable for supporting immobilization of chloroperoxidase (CPO). Firstly, Fe3O4- nanoparticles are deposited on HNT, so magnetic separation can be used instead of centrifugation. Secondly, the magnetic HNT is modified by 3-aminopropyltriethoxysilane (APTES), which can provide amine group on surface of HNT and meanwhile inhibit the agglomeration of magnetic HNT. Then, HNT-Fe3O4 -APTES is linked with branched polyethyleneimine (PEI) to provide more amino for binding with enzyme. The so-prepared resin (CPO-HNT-Fe3O4-APTES-PEI) shows enhanced enzyme loading, reusability, improved thermal stability, and tolerance to organic solvents than free CPO. The affinity and specificity of immobilized enzyme to substrate is increased, Michaelis-Menten kinetic analysis
additional information
-
upon chemical modifications such as modifications of Lys residues with maleic and phthalic anhydride, of carboxyl groups with carbodiimide and ethanolamine or ethylenediamine, crosslinking with DMS and periodate oxidation, the loss of both chlorinating and peroxidative activity is observed for all types of modification, within the range of 39.5 and 56.8% for the chlorinating activity, and 16.4 and 44.5% for peroxidative activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
native CPO and chemically modified CPOs, almost completely stable at room temperature for 3 days
743705
5 - 6.5
-
at pH 6.5 the soluble enzyme retains about 70% of initial activity after 3 days of incubation, while at both pH 6.0 and 5.0 the enzyme retains more than 95%
725740
7.6
-
after 1 h: 50% residual ativity for cross-linked enzyme aggregates, complete inactivation of free enzyme
695425
additional information
7
-
25°C, 24 h, about 50% loss of activity of soluble enzyme, about 40% loss of activity of immobilized enzyme
659741
7
-
native CPO, half-live 5 h. For CPO modified by carbodiimide, ethanolamine and periodate oxidized CPO, half lives are 2.1- and 1.5fold improved
743705
additional information
-
two enzymatically inactive forms obtained at pHs above 7. The first alkaline form obtained between pH 7 and pH 11 is the ferric analog of the ferrous P-420 species. The second alkaline form obtained above pH 11 appears to be a species in which irreversible denaturation has commenced
348313
additional information
-
immobilization of the enzyme on silica gel enhances the stability with respect to the effect of pH and oxidizing agent concentrations
659741
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
the immobilized CPO retains more than 60% of its initial activity after 10 h incubation at 50ºC, while free CPO completely loses its activity. At 70°C, free CPO keeps only about 10% of its initial activity, while immobilized MGO-CPO retains approximately 30% of initial activity after 1 h
70
free CPO can remain only 16.2% of its initial activity after 1 h incubation at 70°C, while the immobilized enzyme can keep almost 100% of activity at the same condition
90
free CPO can remain below 15% of its initial activity after 1 h incubation at 90°C, while the immobilized enzyme can keep about 30% of activity at the same condition
25
35
-
at 35°C, the reaction rate initially increases, but the enzyme rapidly becomes inactivated and the reaction rate decreases
40
40 - 50
-
thermostability is greatly improved in a reverse micelle composed of surfactant-water-isooctane-pentanol: at 40°C, CPO essentially loses all its activity after 5 h incubation, while 58-76% catalytic activity is retained for both reactions in the two reverse micelle media. At 50°C, about 44-75% catalytic activity remains for both reactions in reverse micelle after 2 h compared with no observed activity in pure buffer under the same conditions
45 - 55
-
at 45°C, the conjugated-CPO preserved loses about 7% of its initial activity whereas the free enzyme loses about 34% of its initial activity during a 120 min incubation period. At 55°C, the conjugated-CPO and free CPO retain their activity about to a level of 53% and 11%, respectively
50
60
70
-
1 h, about 10% loss of activity of crystals cross-linked with glutaraldehyde and more than 95% loss of activity of soluble enzyme
80
-
1 h, about 95% loss of activity of crystals cross-linked with glutaraldehyde and complete than 90% loss of activity of soluble enzyme
additional information
25
-
about 95% loss of activity of the pure enzyme in 0.05 M citrate buffer, pH 5, about 60% loss of activity in presence of 0.1 M PEG 200 and PEG 400, about 40% loss of activity in presence of 0.1 M di(ethylene glycol), about 80% loss of activity in presence of 0.1 M di(propylene glycol)
25
-
the activity of CPO is almost demolished in the presence of 0.01 M glucose after only 9 h. Dioctyl sulfosuccinate sodium salt, PEG200, and glycerol exhibit strong stabilizing effect and are capable of preventing CPO from inactivation in the 432 h incubation period
40
-
the stability of CPO is decreased by glucose, fructose, galactose, xylose, dextran, and surfactant dioctyl sulfosuccinate sodium salt. Stability can be increased by PEG200, glycerol, trehalose, and gum sugar. In the absence of the additives, CPO loses almost all of its activity after 90 h. However, in PEG200 solutions, 88.5% activity is retained after 329 h. The storage time of CPO in trehalose and gum sugar can be prolonged to 233 and 113 h, respectively
50
-
1 h, 50% loss of activity of crystals cross-linked with glutaraldehyde and of soluble enzyme
50
-
6 h, native CPO retains about 10% peroxidase activity and 20% sulfoxidation activity in aqueous buffer. CPOs modified by citraconic anhydride, phthalic anhydride or maleic anhydride, retain about 30% peroxidase activity and 30% sulfoxidation activity
50
-
t1/2 of the free enzyme is 148.9 min, t1/2 for immobilized enzyme is 285.7 min
50
-
the native enzyme loses almost all of its activity after 10 h of incubation, in 0.2 M glycerol the enzyme retains activity for up to 200 h. In the presence of 0.05 M PEG200, the enzyme remains as active as freshly prepared samples in the first 10 h. After 192 h of incubation, 13% activity could still be retained. Enzyme retains 24% of its activity after 24 h of standing in dextran-containing buffers
50
-
40% activity after 40 min for immobilized enzyme, 0.02% activity after 40 min for free enzyme
50
-
pH 5.0, native CPO, half-live 2 h. All chemically modified CPOs are more stable than the native CPO
60
-
1 h, about 10% loss of activity of crystals cross-linked with glutaraldehyde and more than 90% loss of activity of soluble enzyme
60
-
activity of CPO is almost completely lost in the first 50 min of incubation in the absence of additives. In the presence of PEG200, trehalose, galactose, glycerol, gum sugar, and dextran, 26.5%, 17.7%, 15.6%, 12.4%, 2.6%, and 1.7%, respectively, of enzyme activity can be rescued
60
-
t1/2 of the free enzyme is 25.6 min, t1/2 for immobilized enzyme is 34.1 min
60
-
after 1 h: approximately 60% residual activity for cross-linked enzyme aggregates, free enzyme is deactivated (<5% residual activity)
additional information
-
crystal crosslinking with glutaraldehyde yields a chloroperoxidase preparation with enhanced thermal resistance compared to soluble enzyme
additional information
-
PEG200 and glycerol are the most efficient stabilizer for CPO in temperatures ranging from 25°C to 60°C
additional information
-
the thermostability of peroxidase of CPO is increased about 2fold upon these chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride. The thermostability of sulfoxidation activity of CPO is increased about 1.2fold upon these chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.3 mM H2O2, 20 h: 58% activity for immobilized enzyme, 43% activity for free enzyme
-
1.5 M urea, 20 h: 99% activity for immobilized enzyme, 68% activity for free enzyme
-
30 mM H2O2, 5 min: 80% residual activity for the cross-linked enzyme aggregates
-
addition of poly(ethylene glycol) results in an increase of 57% for interface-bound CPO and 33% for native enzyme
-
addition of polyethyleneimine results in enhancement of storage stability against H2O2 deactivation, but does not affect the operational stability of the enzyme
-
covalently bonded CPO on the mesoporous material SBA-15 exhibits a higher operational stability in a continuously operated fixed-bed reactor compared to a catalyst prepared by physisorption of the enzyme. Chloroperoxidase immobilization into SBA-15 shows a remaining activity of about 9%
-
cross-linked enzyme aggregates exhibit greatly improved stability in the presence of H2O2
-
crystal crosslinking with glutaraldehyde yields a chloroperoxidase preparation with enhanced thermal resistance compared to soluble enzyme
-
di(ethylene glycol) and di(propylene glycol) stabilize the enzyme towards denaturation by H2O2
-
enzyme immobilized on monoaminoethyl-N-aminoethyl through carbodiimide-coupled method shows an increase in apparent half-life time of more than 500fold that of the soluble enzyme
-
glucose enhances the operational stability by two folds, but exhibits no significant effect on storage stability
-
immobilization of chloroperoxidase to silica gel in order to increase its stability either in buffer solution or in the presence of the oxidant tert-butyl hydroperoxide. The binding between enzyme and silica gel results in a non-homogeneous enzyme population. Existence of three different enzyme populations. Two populations of the immobilized enzyme show an apparent increase in the stability both to the pH or to the presence of the oxidant
-
immobilization of the enzyme on silica gel enhances the stability with respect to the effect of pH and oxidizing agent concentrations
-
immobilized CPO (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) retains 83% of its initial activity after 12 cycles of usage
-
interface-assembled enzyme shows improved stability as compared to native enzyme, enzyme deactivation as a result of the side effect of H2O2, still limits the overall productivity of the enzyme
-
PEG200 and glycerol are the most efficient stabilizer for CPO in temperatures ranging from 25°C to 60°C. Trehalose is more helpful than other sugars for extended storage of CPO
-
stability of the immobilized CPO (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) is improved compared to free form
-
stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide
-
the catalytic efficiency of free CPO is decreased about 1.6fold upon immobilization. The conjugated-CPO activity on the poly(hydroxypropyl)methacrylateco-poly(ethylene glycol)-methacrylate-3 membrane remains almost the same as the original activity after 9 cycles. After that, a steady decrease in chlorination capability of the conjugated-CPO is observed, and this loss reaches about 27% after 25 cycles of batch operation
-
the enzyme tolerates up to 30% v/v 1,3-dimethylimidazolium methylsulfate or 1-butyl-3-methylimidazolium methylsulfate
-
the thermostability of peroxidase of CPO is increased about 2fold upon these chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride. The thermostability of sulfoxidation activity of CPO is increased about 1.2fold upon the chemical modification by citraconic anhydride, phthalic anhydride or maleic anhydride
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,3-dimethylimidazolium methylsulfate
-
the enzyme tolerates up to 30% v/v in citrate buffer system, activity is retained for 24 h
1-butyl-3-methylimidazolium methylsulfate
-
the enzyme tolerates up to 30% v/v in cytitrate buffer system, activity is retained for 24 h
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
tert-butyl hydroperoxide, 10 mM, soluble enzyme is almost completely inactive after 2 h, immobilized enzyme still retains 20% of its activity after 4 h. After 24 h in 0.1 mM tert-butyl hydroperoxide the activity of immobilized enzyme is unaffected, while soluble enzyme loses more than 50% of its original activity
-
659741
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, pH 6.0, half-life of autoxidation of the oxygenated heme protein is 20 min
-
-20°C, pH 6.0, half-life of autoxidation of the oxygenated heme protein is 85 min
-
4°C, citrate buffer (50 mM, pH 3.0), 4 weeks, 91% loss of activity of the soluble enzyme, immobilized (covalent immobilization of chloroperoxidase on the magnetic p(GMA-MMA-EGDMA) beads) enzyme loses 15% of its initial activity
-
4°C, conjugated-CPO in citrate buffer (50 mM, pH 3.0), 8 weeks, the conjugated-CPO preserves its initial activity more than 60%
-
4°C, CPO immobilized into glutaraldehyde-3-aminopropyltrimethoxysilane-SBA-15 in a buffer at pH 3.4, storage results in leaching of the enzyme from the support due to hydrolytic cleavage of the imino bond
-
4°C, CPO immobilized into glutaraldehyde-3-aminopropyltrimethoxysilane-SBA-15 in a buffer at pH 7.0, a few days, complete loss of enzyme activity
-
4°C, free and conjugated-CPO in citrate buffer (50 mM, pH 3.0), 4 weeks, the activity loss of the conjugated-CPO is 7% while the free enzyme loses its initial activity about 83%
-
4°C, free enzyme in citrate buffer (50 mM, pH 3.0), 6 weeks, the free enzyme loses all its activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
rapid and efficient enzymatic decolorization of anthraquinone (alizarin red) and triphenylmethane dyes (crystal violet). The chromophoric groups are destructed and the dye molecules are broken-down into small pieces. The enzyme shows strong toleration to the typical salt species NaCl, NaNO3, and Na2SO4
environmental protection
synthesis
chloroperoxidase (CPO) has long been recognized as a powerful and versatile catalyst, potential of co-immobilized enzymes chloroperoxidase and glucose oxidase as MGO-GOx-CPO in environmental applications
environmental protection
synthesis
environmental protection
amino modified magnetic halloysite nanotube supporting chloroperoxidase immobilization is useful for enhanced stability, reusability, and efficient degradation of pesticide residue in wastewater. Degradation of mesotrione in wastewater by the immobilized CPO
environmental protection
CPO carries out a wide variety of oxidative reactions, changing the environmental impacts of organic matters
environmental protection
-
chloroperoxidase shows oxidative dehalogenation activity and is significantly more robust than other peroxidases and functions under harsher reaction conditions compared to other biocatalysts. Expanding the scope of reactivity achieved by the enzyme may be beneficial for industrial and biotechnological functions in the future. This considerable extension of already known activities could lead to the use of the enzyme as a biocatalyst in the field of bioremediation and a broader understanding of both how peroxidases and cytochrome P450s react with halogenated organic substrates
environmental protection
-
this enzyme may by employed to treat contaminated soil or water prior to discharge
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itoh, N.; Izumi, Y.; Yamada, H.
Haloperoxidase-catalyzed halogenation of nitrogen-containing aromatic heterocycles represented by nucleic bases
Biochemistry
26
282-289
1987
Leptoxyphium fumago
-
Sono, M.; Smith Eble, K.; Dawson, J.H.; Hager, L.P.
Preparation and properties of ferrous chloroperoxidase complexes with dioxygen, nitric oxide, and an alkyl isocyanide. Spectroscopic dissimilarities between the oxygenated forms of chloroperoxidase and cytochrome P-450
J. Biol. Chem.
260
15530-15535
1985
Leptoxyphium fumago
Hashimoto, A.; Pickard, M.A.
Chloroperoxidases from Caldariomyces (= Leptoxyphium) cultures: glycoprotein with variable carbohydrate content and isoenzymic forms
J. Gen. Microbiol.
130
2051-2058
1984
Leptoxyphium fumago
-
Lambeir, A.M.; Dunford, H.B.
A kinetic and spectral study of the alkaline transitions of chloroperoxidase
Arch. Biochem. Biophys.
220
549-556
1983
Leptoxyphium fumago
Libby, R.D.; Thomas, J.A.; Kaiser, L.W.; Hager, L.P.
Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates
J. Biol. Chem.
257
5030-5037
1982
Leptoxyphium fumago
Shahangian, S.; Hager, L.P.
The reaction of chloroperoxidase with chlorite and chlorine dioxide
J. Biol. Chem.
256
6034-6040
1981
Leptoxyphium fumago
Sae, A.S.W.; Cunningham, B.A.
Isolation and properties of chloroperoxidase isozymes
Phytochemistry
18
1785-1787
1979
Leptoxyphium fumago
-
Hallenberg, P.F.; Hager, L.P.
Purification of chloroperoxidase from Caldariomyces fumago
Methods Enzymol.
52
521-529
1978
Leptoxyphium fumago
Morris, D.R.; Hager, L.P.
Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein
J. Biol. Chem.
241
1763-1768
1966
Leptoxyphium fumago
Hager, L.P.; Morris, D.R.; Brown, F.S.; Eberwein, H.
Chloroperoxidase. II. Utilization of halogen anions
J. Biol. Chem.
241
1769-1777
1966
Leptoxyphium fumago
Morris, D.R.; Hager, L.P.
Mechanism of the inhibition of enzymatic halogenation by antithyroid agents
J. Biol. Chem.
241
3582-3589
1966
Leptoxyphium fumago
Carmichael, R.; Fedorak, P.M.; Pickard, M.A.
Oxidation of phenols by chloroperoxidase
Biotechnol. Lett.
7
289-294
1985
Leptoxyphium fumago
-
Dunford, H.B.; Lambeir, A.M.; Kashem, M.A.; Pickard, M.
On the mechanism of chlorination by chloroperoxidase
Arch. Biochem. Biophys.
252
292-302
1987
Leptoxyphium fumago
Fang, G.H.; Kenigsberg, P.; Axley, M.J.; Nuell, M.; Hager, L.P.
Cloning and sequencing of chloroperoxidase cDNA
Nucleic Acids Res.
14
8061-8071
1986
Leptoxyphium fumago
Dawson, J.H.; Kau, L.S.; Penner-Hahn, J.E.; Sono, M.; Smith Eble, K.; Bruce, G.S.; Hager, L.P.; Hodgson, K.O.
Oxygenated cytochrome P-450-CAM and chloroperoxidase: direct evidence for sulfur donor ligation trans to dioxygen and structural characterization using EXAFS spectroscopy
J. Am. Chem. Soc.
108
8114-8116
1986
Leptoxyphium fumago
-
Yamada, H.; Itoh, N.; Izumi, Y.
Chloroperoxidase-catalyzed halogenation of trans-cinnamic acid and its derivatives
J. Biol. Chem.
260
11962-11969
1985
Leptoxyphium fumago
Gonzalez-Vergara, E.; Ales, D.C.; Goff, H.M.
A simple, rapid, high yield isolation and purification procedure for chloroperoxidase isoenzymes
Prep. Biochem.
15
335-348
1985
Leptoxyphium fumago
Conesa, A.; Van de Velde, F.; Van Rantwijk, F.; Sheldon, R.A.; Van den Hondel, C.A.M.J.J.; Punt, P.J.
Expression of the Caldariomyces fumago chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme
J. Biol. Chem.
276
17635-17640
2001
Leptoxyphium fumago
Vazquez-Duhalt, R.; Ayala, M.; Marquez-Rocha, F.J.
Biocatalytic chlorination of aromatic hydrocarbons by chloroperoxidase of Caldariomyces fumago
Phytochemistry
58
929-933
2001
Leptoxyphium fumago
Casella, L.; Poli, S.; Gullotti, M.; Selvaggini, C.; Beringhelli, T.; Marchesini, A.
The chloroperoxidase-catalyzed oxidation of phenols. Mechanism, selectivity, and characterization of enzyme-substrate complexes
Biochemistry
33
6377-6386
1994
Leptoxyphium fumago
Ramakrishnan, K.; Oppenhiuzen, M.E.; Saunders, S.; Fisher, J.
Stereoselectivity of chloroperoxidase-dependent halogenation
Biochemistry
22
3271-3277
1983
Leptoxyphium fumago
La Rotta, C.E.; Bon, E.P.
4-chlorophenol degradation by chloroperoxidase from Caldariomyces fumago: formation of insoluble products
Appl. Biochem. Biotechnol.
98-100
191-203
2002
Leptoxyphium fumago
Torres, E.; Aburto, J.
Chloroperoxidase-catalyzed oxidation of 4,6-dimethyldibenzothiophene as dimer complexes: evidence for kinetic cooperativity
Arch. Biochem. Biophys.
437
224-232
2005
Leptoxyphium fumago
Ayala, M.; Horjales, E.; Pickard, M.A.; Vazquez-Duhalt, R.
Cross-linked crystals of chloroperoxidase
Biochem. Biophys. Res. Commun.
295
828-831
2002
Leptoxyphium fumago
Toti, P.; Petri, A.; Gambicorti, T.; Osman, A.M.; Bauer, C.
Kinetic and stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide
Biophys. Chem.
113
105-113
2005
Leptoxyphium fumago
Sanfilippo, C.; D'Antona, N.; Nicolosi, G.
Chloroperoxidase from Caldariomyces fumago is active in the presence of an ionic liquid as co-solvent
Biotechnol. Lett.
26
1815-1819
2004
Leptoxyphium fumago
Spreti, N.; Germani, R.; Incani, A.; Savelli, G.
Stabilization of chloroperoxidase by polyethylene glycols in aqueous media: kinetic studies and synthetic applications
Biotechnol. Prog.
20
96-101
2004
Leptoxyphium fumago
Holland, H.L.; Brown, F.M.; Lozada, D.; Mayne, B.; Szerminski, W.R.; van Vliet, A.J.
Chloroperoxidase-catalyzed oxidation of methionine derivatives
Can. J. Chem.
80
633-639
2002
Leptoxyphium fumago
-
Yi, X.; Conesa, A.; Punt, P.J.; Hager, L.P.
Examining the role of glutamic acid 183 in chloroperoxidase catalysis
J. Biol. Chem.
278
13855-13859
2003
Leptoxyphium fumago
Zhu, G.; Wang, P.
Novel interface-binding chloroperoxidase for interfacial epoxidation of styrene
J. Biotechnol.
117
195-202
2005
Leptoxyphium fumago
Petri, A.; Gambicorti, T.; Salvadori, P.
Covalent immobilization of chloroperoxidase on silica gel and properties of the immobilized biocatalyst
J. Mol. Catal. B
27
103-106
2004
Leptoxyphium fumago
-
Hu, S.; Dordick, J.S.
Highly enantioselective oxidation of cis-cyclopropylmethanols to corresponding aldehydes catalyzed by chloroperoxidase
J. Org. Chem.
67
314-317
2002
Leptoxyphium fumago
Speicher, A.; Heisel, R.; Kolz, J.
First detection of a chloroperoxidase in bryophytes
Phytochemistry
62
679-682
2003
Leptoxyphium fumago, Bazzania trilobata
Sanfilippo, C.; Nicolosi, G.
Catalytic behavior of chloroperoxidase from Caldariomyces fumago in the oxidation of cyclic conjugated dienes
Tetrahedron
13
1889-1892
2002
Leptoxyphium fumago
-
Bougioukou, D.J.; Smonou, I.
Chloroperoxidase-catalyzed oxidation of conjugated dienoic esters
Tetrahedron Lett.
43
339-342
2002
Leptoxyphium fumago
-
Hofrichter, M.; Ullrich, R.
Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance
Appl. Microbiol. Biotechnol.
71
276-288
2006
Leptoxyphium fumago
Kaup, B.A.; Piantini, U.; Wuest, M.; Schrader, J.
Monoterpenes as novel substrates for oxidation and halo-hydroxylation with chloroperoxidase from Caldariomyces fumago
Appl. Microbiol. Biotechnol.
73
1087-1096
2007
Leptoxyphium fumago
Bhakta, M.N.; Wimalasena, K.
A mechanistic comparison between cytochrome P450- and chloroperoxidase-catalyzed N-dealkylation of N,N-dialkyl anilines
Eur. J. Org. Chem.
(2005)
4801-4805
2005
Leptoxyphium fumago
-
Osborne, R.L.; Raner, G.M.; Hager, L.P.; Dawson, J.H.
C. fumago chloroperoxidase is also a dehaloperoxidase: oxidative dehalogenation of halophenols
J. Am. Chem. Soc.
128
1036-1037
2006
Leptoxyphium fumago
Kuehnel, K.; Blankenfeldt, W.; Terner, J.; Schlichting, I.
Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate
J. Biol. Chem.
281
23990-23998
2006
Leptoxyphium fumago
Narayanan, R.; Zhu, G.; Wang, P.
Stabilization of interface-binding chloroperoxidase for interfacial biotransformation
J. Biotechnol.
128
86-92
2007
Leptoxyphium fumago
Toti, P.; Petri, A.; Gambicorti, T.; Osman, A.M.; Bauer, C.
Inactivation studies on native and silica gel non-homogeneous immobilized chloroperoxidase
J. Mol. Catal. B
38
65-72
2006
Leptoxyphium fumago
-
Stone, K.L.; Behan, R.K.; Green, M.T.
Resonance Raman spectroscopy of chloroperoxidase compound II provides direct evidence for the existence of an iron(IV)-hydroxide
Proc. Natl. Acad. Sci. USA
103
12307-12310
2006
Leptoxyphium fumago
Kuehnel, K.; Derat, E.; Terner, J.; Shaik, S.; Schlichting, I.
Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes
Proc. Natl. Acad. Sci. USA
104
99-104
2007
Leptoxyphium fumago
Chiappe, C.; Neri, L.; Pieraccini, D.
Application of hydrophilic ionic liquids as co-solvents in chloroperoxidase catalyzed oxidations
Tetrahedron Lett.
47
5089-5093
2006
Leptoxyphium fumago
-
Denisov, I.G.; Dawson, J.H.; Hager, L.P.; Sligar, S.G.
The ferric-hydroperoxo complex of chloroperoxidase
Biochem. Biophys. Res. Commun.
363
954-958
2007
Leptoxyphium fumago
Bayramoglu, G.; Kiralp, S.; Yilmaz, M.; Toppare, L.; Arica, M.Y.
Covalent immobilization of chloroperoxidase onto magnetic beads: Catalytic properties and stability
Biochem. Eng. J.
38
180-188
2008
Leptoxyphium fumago
-
Manoj, K.M.; Hager, L.P.
Chloroperoxidase, a janus enzyme
Biochemistry
47
2997-3003
2008
Leptoxyphium fumago
Murphy, C.D.
Fluorophenol oxidation by a fungal chloroperoxidase
Biotechnol. Lett.
29
45-49
2007
Leptoxyphium fumago
Zhi, L.; Jiang, Y.; Wang, Y.; Hu, M.; Li, S.; Ma, Y.
Effects of additives on the thermostability of chloroperoxidase
Biotechnol. Prog.
23
729-733
2007
Leptoxyphium fumago
Longoria, A.; Tinoco, R.; Vazquez-Duhalt, R.
Chloroperoxidase-mediated transformation of highly halogenated monoaromatic compounds
Chemosphere
72
485-490
2008
Leptoxyphium fumago
Aguila, S.; Vazquez-Duhalt, R.; Tinoco, R.; Rivera, M.; Pecchi, G.; Alderete, J.B.
Stereoselective oxidation of R-(+)-limonene by chloroperoxidase from Caldariomyces fumago
Green Chem.
10
647-653
2008
Leptoxyphium fumago
-
Osborne, R.L.; Coggins, M.K.; Terner, J.; Dawson, J.H.
Caldariomyces fumago chloroperoxidase catalyzes the oxidative dehalogenation of chlorophenols by a mechanism involving two one-electron steps
J. Am. Chem. Soc.
129
14838-14839
2007
Leptoxyphium fumago
Grey, C.E.; Rundbaeck, F.; Adlercreutz, P.
Improved operational stability of chloroperoxidase through use of antioxidants
J. Biotechnol.
135
196-201
2008
Leptoxyphium fumago
Gebicka, L.; Didik, J.
Kinetic studies of the reaction of heme-thiolate enzyme chloroperoxidase with peroxynitrite
J. Inorg. Biochem.
101
159-164
2007
Leptoxyphium fumago
Perez, D.; Van Rantwijk, F.; Sheldon, R.
Cross-linked enzyme aggregates of chloroperoxidase: synthesis, optimization and characterization
Adv. Synth. Catal.
351
2133-2139
2009
Leptoxyphium fumago
-
Longoria, A.M.; Hu, H.; Vazquez-Duhalt, R.
Enzymatic synthesis of semiconductor polymers by chloroperoxidase of Caldariomyces fumago
Appl. Biochem. Biotechnol.
162
927-934
2010
Leptoxyphium fumago, Leptoxyphium fumago 98362
Aburto, J.; Correa-Basurto, J.; Torres, E.
Atypical kinetic behavior of chloroperoxidase-mediated oxidative halogenation of polycyclic aromatic hydrocarbons
Arch. Biochem. Biophys.
480
33-40
2008
Leptoxyphium fumago
Lindborg, J.; Tanskanen, A.; Kanerva, L.
Chemoselective chloroperoxidase-catalyzed oxidation of hexen-1-ols
Biocatal. Biotransform.
27
204-210
2009
Leptoxyphium fumago
-
Gruia, F.; Ionascu, D.; Kubo, M.; Ye, X.; Dawson, J.; Osborne, R.L.; Sligar, S.G.; Denisov, I.; Das, A.; Poulos, T.L.; Terner, J.; Champion, P.M.
Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy
Biochemistry
47
5156-5167
2008
Leptoxyphium fumago
Zhang, L.H.; Bai, C.H.; Wang, Y.S.; Jiang, Y.C.; Hu, M.C.; Li, S.N.; Zhai, Q.G.
Improvement of chloroperoxidase stability by covalent immobilization on chitosan membranes
Biotechnol. Lett.
31
1269-1272
2009
Leptoxyphium fumago
Diaz-Diaz, G.; Bianco-Lopez, M.; Lobo-Castanon, M.; Miranda-Ordieres, A.; Tunon-Blanco, P.
Chloroperoxidase modified electrode for amperometric determination of 2,4,6-trichlorophenol
Electroanalysis
21
1348-1353
2009
Leptoxyphium fumago
-
Tzialla, A.; Kalogeris, E.; Gournis, D.; Sanakis, Y.; Stamatis, H.
Enhanced catalytic performance and stability of chloroperoxidase from Caldariomyces fumago in surfactant free ternary water-organic solvent systems
J. Mol. Catal. B
51
24-35
2008
Leptoxyphium fumago
-
Roberge, C.; Amos, D.; Pollard, D.; Devine, P.
Preparation and application of cross-linked aggregates of chloroperoxidase with enhanced hydrogen peroxide tolerance
J. Mol. Catal. B
56
41-45
2009
Leptoxyphium fumago
-
Lai, W.; Chen, H.; Cho, K.B.; Shaik, S.
Effects of Substrate, Protein Environment, and Proximal Ligand Mutation on Compound I and Compound 0 of Chloroperoxidase
J. Phys. Chem. A
113
11763-11771
2009
Aspergillus niger, Leptoxyphium fumago
Chen, H.; Hirao, H.; Derat, E.; Schlichting, I.; Shaik, S.
Quantum mechanical/molecular mechanical study on the mechanisms of compound I formation in the catalytic cycle of chloroperoxidase: an overview on heme enzymes
J. Phys. Chem. B
112
9490-9500
2008
Leptoxyphium fumago
Lai, W.; Chen, H.; Shaik, S.
What kinds of ferryl species exist for compound II of chloroperoxidase? A dialog of theory with experiment
J. Phys. Chem. B
113
7912-7917
2009
Leptoxyphium fumago
Bayramoglu, G.; Altintas, B.; Yilmaz, M.; Arica, M.Y.
Immobilization of chloroperoxidase onto highly hydrophilic polyethylene chains via bio-conjugation: Catalytic properties and stabilities
Bioresour. Technol.
102
475-482
2010
Leptoxyphium fumago
Jung, D.; Streb, C.; Hartmann, M.
Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve SBA-15
Int. J. Mol. Sci.
11
762-778
2010
Leptoxyphium fumago
Ayala, M.; Batista, C.V.; Vazquez-Duhalt, R.
Heme destruction, the main molecular event during the peroxide-mediated inactivation of chloroperoxidase from Caldariomyces fumago
J. Biol. Inorg. Chem.
16
63-68
2011
Leptoxyphium fumago
Wang, Y.; Wu, J.; Ru, X.; Jiang, Y.; Hu, M.; Li, S.; Zhai, Q.
Catalytic performance and thermostability of chloroperoxidase in reverse micelle: achievement of a catalytically favorable enzyme conformation
J. Ind. Microbiol. Biotechnol.
38
717-724
2011
Leptoxyphium fumago
Diaz-Diaz, G.; Blanco-Lopez, M.; Lobo-Castanon, M.; Miranda-Ordieres, A.; Tunon-Blanco, P.
Kinetic study of the oxidative dehalogenation of 2,4,6-trichlorophenol catalyzed by chloroperoxidase
J. Mol. Catal. B
66
332-336
2010
Leptoxyphium fumago
-
de Hoog, H.M.; Nallani, M.; Cornelissen, J.J.; Rowan, A.E.; Nolte, R.J.; Arends, I.W.
Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors
Org. Biomol. Chem.
7
4604-4610
2009
Leptoxyphium fumago
Andrew, D.; Hager, L.; Manoj, K.M.
The intriguing enhancement of chloroperoxidase mediated one-electron oxidations by azide, a known active-site ligand
Biochem. Biophys. Res. Commun.
415
646-649
2011
Leptoxyphium fumago
Zhang, R.; He, Q.; Chatfield, D.; Wang, X.
Paramagnetic nuclear magnetic resonance relaxation and molecular mechanics studies of the chloroperoxidase-indole complex: Insights into the mechanism of chloroperoxidase-catalyzed regioselective oxidation of indole
Biochemistry
52
3688-3701
2013
Leptoxyphium fumago
-
Buchhaupt, M.; Ehrich, K.; Huettmann, S.; Guder, J.; Schrader, J.
Over-expression of chloroperoxidase in Caldariomyces fumago
Biotechnol. Lett.
33
2225-2231
2011
Leptoxyphium fumago, Leptoxyphium fumago DSM 1256
Popiel, S.; Nawala, J.
Detoxification of sulfur mustard by enzyme-catalyzed oxidation using chloroperoxidase
Enzyme Microb. Technol.
53
295-301
2013
Leptoxyphium fumago
Pesic, M.; Lopez, C.; Alvaro, G.; Lopez-Santin, J.
A novel immobilized chloroperoxidase biocatalyst with improved stability for the oxidation of amino alcohols to amino aldehydes
J. Mol. Catal. B
84
144-151
2012
Leptoxyphium fumago
-
Morozov, A.N.; Chatfield, D.C.
Chloroperoxidase-catalyzed epoxidation of cis-beta-methylstyrene: distal pocket flexibility tunes catalytic reactivity
J. Phys. Chem. B
116
12905-12914
2012
Leptoxyphium fumago
Li, H.; Gao, J.; Wang, L.; Li, X.; Jiang, Y.; Hu, M.; Li, S.; Zhai, Q.
Promotion of activity and thermal stability of chloroperoxidase by trace amount of metal ions (M2+/M3+)
Appl. Biochem. Biotechnol.
172
2338-2347
2014
Leptoxyphium fumago (P04963)
-
Zhang, R.; He, Q.; Huang, Y.; Wang, X.
Spectroscopic and QM/MM investigations of chloroperoxidase catalyzed degradation of orange G
Arch. Biochem. Biophys.
596
1-9
2016
Leptoxyphium fumago, Leptoxyphium fumago ATCC 16373
Liu, L.; Zhang, J.; Tan, Y.; Jiang, Y.; Hu, M.; Li, S.; Zhai, Q.
Rapid decolorization of anthraquinone and triphenylmethane dye using chloroperoxidase Catalytic mechanism, analysis of products and degradation route
Chem. Eng. J.
244
9-18
2014
Leptoxyphium fumago (P04963)
-
Getrey, L.; Krieg, T.; Hollmann, F.; Schrader, J.; Holtmann, D.
Enzymatic halogenation of the phenolic monoterpenes thymol and carvacrol with chloroperoxidase
Green Chem.
16
1104-1108
2014
Leptoxyphium fumago (P04963)
-
Buchhaupt, M.; Huettmann, S.; Sachs, C.C.; Bormann, S.; Hannappel, A.; Schrader, J.
Caldariomyces fumago DSM1256 contains two chloroperoxidase genes, both encoding secreted and active enzymes
J. Mol. Microbiol. Biotechnol.
25
237-243
2015
Leptoxyphium fumago (A0A0A7RMU1), Leptoxyphium fumago, Leptoxyphium fumago DSM 1256 (A0A0A7RMU1)
Pesic, M.; Bozic, N.; Lopez, C.; Loncar, N.; Alvaro, G.; Vujcic, Z.
Chemical modification of chloroperoxidase for enhanced stability and activity
Process Biochem.
49
1472-1479
2014
Leptoxyphium fumago
-
Masdeu, G.; Perez-Trujillo, M.; Lopez-Santin, J.; Alvaro, G.
Chloroperoxidase-catalyzed amino alcohol oxidation Substrate specificity and novel strategy for the synthesis of N-Cbz-3-aminopropanal
Process Biochem.
51
1204-1211
2016
Leptoxyphium fumago
-
Garcia-Embid, S.; Di Renzo, F.; De Matteis, L.; Spreti, N.; M. de la Fuente, J.
Magnetic separation and high reusability of chloroperoxidase entrapped in multi polysaccharide micro-supports
Appl. Catal. B
560
94-102
2018
Leptoxyphium fumago (P04963)
-
Gao, F.; Guo, Y.; Fan, X.; Hu, M.; Li, S.; Zhai, Q.; Jiang, Y.; Wang, X.
Enhancing the catalytic performance of chloroperoxidase by co-immobilization with glucose oxidase on magnetic graphene oxide
Biochem. Eng. J.
143
101-109
2019
Leptoxyphium fumago (P04963)
-
Zhu, X.; Fan, X.; Wang, Y.; Zhai, Q.; Hu, M.; Li, S.; Jiang, Y.
Amino modified magnetic halloysite nanotube supporting chloroperoxidase immobilization enhanced stability, reusability, and efficient degradation of pesticide residue in wastewater
Bioprocess Biosyst. Eng.
44
483-493
2021
Leptoxyphium fumago (P04963)
Wang, K.; Huang, X.; Lin, K.
Multiple catalytic roles of chloroperoxidase in the transformation of phenol products and pathways
Ecotoxicol. Environ. Saf.
179
96-103
2019
Leptoxyphium fumago (P04963)
Chen, Y.; Lin, K.; Chen, D.; Wang, K.; Zhou, W.; Wu, Y.; Huang, X.
Formation of environmentally relevant polyhalogenated carbazoles from chloroperoxidase-catalyzed halogenation of carbazole
Environ. Pollut.
232
264-273
2018
Leptoxyphium fumago (P04963)
Thiel, D.; Blume, F.; Jaeger, C.; Deska, J.
Chloroperoxidase-Catalyzed Achmatowicz Rearrangements
Eur. J. Org. Chem.
2018
2717-2725
2018
Leptoxyphium fumago (P04963)
-
He, J.; Zhang, Y.; Yuan, Q.; Liang, H.
Catalytic activity and application of immobilized chloroperoxidase by biometric magnetic nanoparticles
Ind. Eng. Chem. Res.
58
3555-3560
2019
Leptoxyphium fumago (P04963)
-
Ghorbani Sangoli, M.; Housaindokht, M.R.; Bozorgmehr, M.R.
Effects of the deglycosylation on the structure and activity of chloroperoxidase molecular dynamics simulation approach
J. Mol. Graph. Model.
97
107570
2020
Leptoxyphium fumago (P04963)
Ghorbani, S.; Housaindokht, M.; Bozorgmehr, M.
Investigating the effect of 1-butyl-3-methylimidazolium bromide and 1-butyl-3-methylimidazolium methyl sulfate ionic liquids on structure and function of chloroproxidase by molecular dynamics simulation
J. Mol. Liq.
332
115850
2021
Leptoxyphium fumago (P04963)
-
Chatfield, D.C.; Morozov, A.N.
Proximal pocket controls alkene oxidation selectivity of cytochrome P450 and chloroperoxidase toward small, nonpolar substrates
J. Phys. Chem. B
122
7828-7838
2018
Leptoxyphium fumago (P04963)
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